Biochemical nature of Russell Bodies

Maria Francesca Mossuto, Diletta Ami, Tiziana Anelli, Claudio Fagioli, Silvia Maria Doglia, Roberto Sitia

Research output: Contribution to journalArticlepeer-review

Abstract

Professional secretory cells produce and release abundant proteins. Particularly in case of mutations and/or insufficient chaperoning, these can aggregate and become toxic within or amongst cells. Immunoglobulins (Ig) are no exception. In the extracellular space, certain Ig-L chains form fibrils causing systemic amyloidosis. On the other hand, Ig variants lacking the first constant domain condense in dilated cisternae of the early secretory compartment, called Russell Bodies (RB), frequently observed in plasma cell dyscrasias, autoimmune diseases and chronic infections. RB biogenesis can be recapitulated in lymphoid and non-lymphoid cells by expressing mutant Ig-Î 1/4, providing powerful models to investigate the pathophysiology of endoplasmic reticulum storage disorders. Here we analyze the aggregation propensity and the biochemical features of the intra- and extra-cellular Ig deposits in human cells, revealing β-aggregated features for RB.

Original languageEnglish
Article number12585
JournalScientific Reports
Volume5
DOIs
Publication statusPublished - Jul 30 2015

ASJC Scopus subject areas

  • General

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